Protein O-Mannose Kinase enables Like-acetyl-glucosaminyltransferase 1 to elongate matriglycan on α-dystroglycan, thereby allowing matriglycan to function as a scaffold for extracellular matrix proteins and prevent muscular dystrophy.
Rescue of DUX4-induced muscle pathology by the RET inhibitor Sunitinib reveals the therapeutic potential for treatment of Facioscapulohumeral muscular dystrophy using tyrosine kinase inhibitors.
Expression of the disease gene DUX4 inhibits RNA quality control in skeletal muscle, thereby stabilizing thousands of aberrant RNAs, including its own transcript.
The myopathic transcription factor DUX4 induces discordant dysregulation of transcript and protein levels, demonstrating a key role for post-transcriptional gene regulation in facioscapulohumeral muscular dystrophy.
Thrombospondin proteins regulate vesicular trafficking of integrins and other membrane attachment complex proteins to the plasma membrane of skeletal muscle, which provides greater stability and resistance to muscular dystrophy.
While Notch activation dedifferentiates newly differentiated muscle cells; it improves the function of muscle fiber as a niche-supporting cell of muscle stem cells.
A multidisciplinary approach was used to translate the mathematical analysis of Dystrophin movements inside muscle cells into the biology of how Dystrophin interacts with the cell membrane.
The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.
